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Conserved domains on  [gi|254568998|ref|XP_002491609|]
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Hypothetical protein PAS_chr2-1_0682 [Komagataella phaffii GS115]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TMF_TATA_bd pfam12325
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ...
 654-763 2.08e-30

TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.


:

Pssm-ID: 432481 [Multi-domain]  Cd Length: 115  Bit Score: 115.72  E-value: 2.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  654 SGHPTNHAMDMLTSQLRSLELQVSKLKTENKYLAEEKKGLTQEIVKLMKLNENSKAYHHEIETLNQQLQDSKTEYENALI 733
Cdd:pfam12325   6 GAGPSVQLVERLSSTIRRLEGELASLKEELARLEAQRDEARQEIVKLMKENEELKELKKELEELEKELKELEQRYETTLE 85

                          90       100       110
                  ....*....|....*....|....*....|
gi 254568998  734 LLGEKSELVEELRADVEDLKDICKQQVKDM 763
Cdd:pfam12325  86 LLGEKSEEVEELKADVEDLKEMYREQVQQL 115
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 274-561 2.45e-09

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 60.85  E-value: 2.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   274 QKKLEAKELQVKELLEEgmkLSSNEVSLLQTVKRLKQENNSLANELNNASEINRKLESRSQKLDA-LEKEFIKEEDLASK 352
Cdd:TIGR02169  669 SRSEPAELQRLRERLEG---LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeEEKLKERLEELEED 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   353 YDQLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIRELseknihlqsSRDQALSELRECELLLStskaeagvaikKLKE 432
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL---------EARLSHSRIPEIQAELS-----------KLEE 805

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   433 EILSLEERIEVLRVAnENSKQFEKsdnlENYEQLQQEFSHSQENWKLIEDGYIRKISSLESDISSSKTKEQQSGKQVKAL 512
Cdd:TIGR02169  806 EVSRIEARLREIEQK-LNRLTLEK----EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 254568998   513 TSEIKELSRDNTRLINDVQVLSKDISVLKKELNLKNAEIKALNETLENK 561
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
 
Name Accession Description Interval E-value
TMF_TATA_bd pfam12325
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ...
 654-763 2.08e-30

TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.


Pssm-ID: 432481 [Multi-domain]  Cd Length: 115  Bit Score: 115.72  E-value: 2.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  654 SGHPTNHAMDMLTSQLRSLELQVSKLKTENKYLAEEKKGLTQEIVKLMKLNENSKAYHHEIETLNQQLQDSKTEYENALI 733
Cdd:pfam12325   6 GAGPSVQLVERLSSTIRRLEGELASLKEELARLEAQRDEARQEIVKLMKENEELKELKKELEELEKELKELEQRYETTLE 85

                          90       100       110
                  ....*....|....*....|....*....|
gi 254568998  734 LLGEKSELVEELRADVEDLKDICKQQVKDM 763
Cdd:pfam12325  86 LLGEKSEEVEELKADVEDLKEMYREQVQQL 115
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 274-561 2.45e-09

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 60.85  E-value: 2.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   274 QKKLEAKELQVKELLEEgmkLSSNEVSLLQTVKRLKQENNSLANELNNASEINRKLESRSQKLDA-LEKEFIKEEDLASK 352
Cdd:TIGR02169  669 SRSEPAELQRLRERLEG---LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeEEKLKERLEELEED 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   353 YDQLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIRELseknihlqsSRDQALSELRECELLLStskaeagvaikKLKE 432
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL---------EARLSHSRIPEIQAELS-----------KLEE 805

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   433 EILSLEERIEVLRVAnENSKQFEKsdnlENYEQLQQEFSHSQENWKLIEDGYIRKISSLESDISSSKTKEQQSGKQVKAL 512
Cdd:TIGR02169  806 EVSRIEARLREIEQK-LNRLTLEK----EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 254568998   513 TSEIKELSRDNTRLINDVQVLSKDISVLKKELNLKNAEIKALNETLENK 561
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 302-577 3.61e-09

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 3.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 302 LQTVKRLKqENNSLANELNNASEINRKLESRSQKLDALEKEFIKE-EDLASKYDQLKNEFQQKEKELKKVQVRETNLDNK 380
Cdd:COG1196  218 LKEELKEL-EAELLLLKLRELEAELEELEAELEELEAELEELEAElAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 381 LHNANQEIRELSEKNIHLQSSRDQALSELREcellLSTSKAEAGVAIKKLKEEILSLEERIEVLRVANENSKQfeksdNL 460
Cdd:COG1196  297 LARLEQDIARLEERRRELEERLEELEEELAE----LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE-----AL 367

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 461 ENYEQLQQEFSHSQENWKLIEDGYIRKISSLESDISSSKTKEQQSGKQVKALTSEIKELSRDNTRLINDVQVLSKDISVL 540
Cdd:COG1196  368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 254568998 541 KKELNLKNAEIKALNETLENKVNTFDLEKKRLIRKLE 577
Cdd:COG1196  448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
306-554 1.31e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 306 KRLKQENNSLANELNNASEINRKLESRSQKLDALEKEFIKEEDLASKYDQLKNEFQQKEKELKKVQVRETNLDNKLHNAN 385
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 386 QEIRELSEKNIHLQSSRDQALSELRecellLSTSKAEAGVAIKKLKEEILSLEERIEVL--RVANENSKQFEKSDNLENY 463
Cdd:PRK03918 273 KEIEELEEKVKELKELKEKAEEYIK-----LSEFYEEYLDELREIEKRLSRLEEEINGIeeRIKELEEKEERLEELKKKL 347

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 464 EQLQQEFSHSQENWKLIEDgyirkisSLESDISSSKTKEQQSGKQVKALTSEIKELSRDNTRLINDVQVLSKDISVLKKE 543
Cdd:PRK03918 348 KELEKRLEELEERHELYEE-------AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420

                        250
                 ....*....|.
gi 254568998 544 LNLKNAEIKAL 554
Cdd:PRK03918 421 IKELKKAIEEL 431
TMF_DNA_bd pfam12329
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ...
 271-347 2.57e-06

TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes that contains at its N-terminal section a number of leucine zippers that could potentially form coiled coil structures.. The whole proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells.


Pssm-ID: 372049 [Multi-domain]  Cd Length: 74  Bit Score: 45.76  E-value: 2.57e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254568998  271 NNLQKKLEAKELQVKELLEEGMKLSSNEVSLLQTVKRLKQENNSLANELNNASeinRKLESRSQKLDALEKEFIKEE 347
Cdd:pfam12329   1 SSLEKLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELK---KKLEKLEKELENLEERLKRAE 74
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 392-754 4.96e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 4.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   392 SEKNIHLQSSRDQALSELRECELLLSTSKAEAGVAIKKLKEEILSLEERIEVLRVAnENSKQFEKSDNLENYEQLQQEFS 471
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE-LEELSRQISALRKDLARLEAEVE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   472 HSQENWKLIEdgyiRKISSLESDISSSKTKEQQSGKQVKALTSEIKELSRDNTRLINDVQVLSKDISVLKKELNLKNAEI 551
Cdd:TIGR02168  744 QLEERIAQLS----KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   552 KALNETLENKVNTFDLEKKRLIRKLEVKNFPSSDPGIPSDSLSRERSLGDISSTSITSSLNptnnsshnsfqlgESSSRR 631
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN-------------ERASLE 886

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   632 ISTASILDNSFTNDSDVRTIDDSGHPTNHAMDMLTSQLRSLELQVSKLKTE----NKYLAEEKKGLTQEIVKLMKLNENS 707
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRidnlQERLSEEYSLTLEEAEALENKIEDD 966

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 254568998   708 KAY-HHEIETLNQQLQ-------DSKTEYEnalillgEKSELVEELRADVEDLKD 754
Cdd:TIGR02168  967 EEEaRRRLKRLENKIKelgpvnlAAIEEYE-------ELKERYDFLTAQKEDLTE 1014
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 266-448 3.16e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.39  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   266 RDSVINNLQKKLEakelQVKELLEEGMKLSSNEVSLLQTVK-RLKQENNSLANELNNASEINRKLESRSQKLDALEKEFI 344
Cdd:smart00787 138 RMKLLEGLKEGLD----ENLEGLKEDYKLLMKELELLNSIKpKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKL 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   345 KEEDLASKYdqLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIRELSEKnihLQSSRDQALSELRECELLLSTSKAEAG 424
Cdd:smart00787 214 KKLLQEIMI--KVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKK---LEQCRGFTFKEIEKLKEQLKLLQSLTG 288

                          170       180
                   ....*....|....*....|....
gi 254568998   425 VAIKKLKEEILSLEERIEVLRVAN 448
Cdd:smart00787 289 WKITKLSGNTLSMTYDREINLVFD 312
 
Name Accession Description Interval E-value
TMF_TATA_bd pfam12325
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ...
 654-763 2.08e-30

TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.


Pssm-ID: 432481 [Multi-domain]  Cd Length: 115  Bit Score: 115.72  E-value: 2.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  654 SGHPTNHAMDMLTSQLRSLELQVSKLKTENKYLAEEKKGLTQEIVKLMKLNENSKAYHHEIETLNQQLQDSKTEYENALI 733
Cdd:pfam12325   6 GAGPSVQLVERLSSTIRRLEGELASLKEELARLEAQRDEARQEIVKLMKENEELKELKKELEELEKELKELEQRYETTLE 85

                          90       100       110
                  ....*....|....*....|....*....|
gi 254568998  734 LLGEKSELVEELRADVEDLKDICKQQVKDM 763
Cdd:pfam12325  86 LLGEKSEEVEELKADVEDLKEMYREQVQQL 115
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 274-561 2.45e-09

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 60.85  E-value: 2.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   274 QKKLEAKELQVKELLEEgmkLSSNEVSLLQTVKRLKQENNSLANELNNASEINRKLESRSQKLDA-LEKEFIKEEDLASK 352
Cdd:TIGR02169  669 SRSEPAELQRLRERLEG---LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeEEKLKERLEELEED 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   353 YDQLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIRELseknihlqsSRDQALSELRECELLLStskaeagvaikKLKE 432
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL---------EARLSHSRIPEIQAELS-----------KLEE 805

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   433 EILSLEERIEVLRVAnENSKQFEKsdnlENYEQLQQEFSHSQENWKLIEDGYIRKISSLESDISSSKTKEQQSGKQVKAL 512
Cdd:TIGR02169  806 EVSRIEARLREIEQK-LNRLTLEK----EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 254568998   513 TSEIKELSRDNTRLINDVQVLSKDISVLKKELNLKNAEIKALNETLENK 561
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 302-577 3.61e-09

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 3.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 302 LQTVKRLKqENNSLANELNNASEINRKLESRSQKLDALEKEFIKE-EDLASKYDQLKNEFQQKEKELKKVQVRETNLDNK 380
Cdd:COG1196  218 LKEELKEL-EAELLLLKLRELEAELEELEAELEELEAELEELEAElAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 381 LHNANQEIRELSEKNIHLQSSRDQALSELREcellLSTSKAEAGVAIKKLKEEILSLEERIEVLRVANENSKQfeksdNL 460
Cdd:COG1196  297 LARLEQDIARLEERRRELEERLEELEEELAE----LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE-----AL 367

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 461 ENYEQLQQEFSHSQENWKLIEDGYIRKISSLESDISSSKTKEQQSGKQVKALTSEIKELSRDNTRLINDVQVLSKDISVL 540
Cdd:COG1196  368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 254568998 541 KKELNLKNAEIKALNETLENKVNTFDLEKKRLIRKLE 577
Cdd:COG1196  448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 331-577 3.85e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.46  E-value: 3.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   331 SRSQKLDALEKEF----IKEEDLASKYDQLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIREL---SEKNIHLQSSRD 403
Cdd:TIGR02168  674 ERRREIEELEEKIeeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   404 QALSELRECELLLSTSKAEAGVAIKKLKEEILSLEERIEVLRvaNENSKQFEKSDNLENYEQLQQEFSHSQENwkLIEDG 483
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK--EELKALREALDELRAELTLLNEEAANLRE--RLESL 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   484 YIRKISSLESDISSSKTKEQQSGkQVKALTSEIKELSRDNTRLINDVQVLSKDISVLKKELNLKNAEIkalnETLENKVN 563
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSE-DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL----EELSEELR 904

                          250
                   ....*....|....
gi 254568998   564 TFDLEKKRLIRKLE 577
Cdd:TIGR02168  905 ELESKRSELRRELE 918
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 305-569 1.12e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 305 VKRLKQENNSLANELNNASEINRKLESRSQKLDALEKEFIKE----EDLASKYDQLKNEFQQKEKELKKVQVRETNLDNK 380
Cdd:COG1196  231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELrlelEELELELEEAQAEEYELLAELARLEQDIARLEER 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 381 LHNANQEIRELSEKNIHLQSSRDQALSELRECELLLSTSKAEAGVAIKKLKEEILSLEERIEvlRVANENSKQFEKSDNL 460
Cdd:COG1196  311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA--ELAEAEEELEELAEEL 388

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 461 ENYEQLQQEFSHSQENWKLIEDGYIRKISSLESDISSSKTKEQQSGKQVKALTSEIKELSRDNTRLINDVQVLSKDISVL 540
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                        250       260
                 ....*....|....*....|....*....
gi 254568998 541 KKELNLKNAEIKALNETLENKVNTFDLEK 569
Cdd:COG1196  469 LEEAALLEAALAELLEELAEAAARLLLLL 497
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
306-554 1.31e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 306 KRLKQENNSLANELNNASEINRKLESRSQKLDALEKEFIKEEDLASKYDQLKNEFQQKEKELKKVQVRETNLDNKLHNAN 385
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 386 QEIRELSEKNIHLQSSRDQALSELRecellLSTSKAEAGVAIKKLKEEILSLEERIEVL--RVANENSKQFEKSDNLENY 463
Cdd:PRK03918 273 KEIEELEEKVKELKELKEKAEEYIK-----LSEFYEEYLDELREIEKRLSRLEEEINGIeeRIKELEEKEERLEELKKKL 347

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 464 EQLQQEFSHSQENWKLIEDgyirkisSLESDISSSKTKEQQSGKQVKALTSEIKELSRDNTRLINDVQVLSKDISVLKKE 543
Cdd:PRK03918 348 KELEKRLEELEERHELYEE-------AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420

                        250
                 ....*....|.
gi 254568998 544 LNLKNAEIKAL 554
Cdd:PRK03918 421 IKELKKAIEEL 431
TMF_DNA_bd pfam12329
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ...
 271-347 2.57e-06

TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes that contains at its N-terminal section a number of leucine zippers that could potentially form coiled coil structures.. The whole proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells.


Pssm-ID: 372049 [Multi-domain]  Cd Length: 74  Bit Score: 45.76  E-value: 2.57e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254568998  271 NNLQKKLEAKELQVKELLEEGMKLSSNEVSLLQTVKRLKQENNSLANELNNASeinRKLESRSQKLDALEKEFIKEE 347
Cdd:pfam12329   1 SSLEKLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELK---KKLEKLEKELENLEERLKRAE 74
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 263-469 4.02e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.40  E-value: 4.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  263 VNNRDSVINNLQKKLEAKELQVKELLEEGMKLSSNEVSLLQTVKRLKQENNSLANELNNASE-----------INRKLES 331
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdsvkeliiknLDNTRES 465

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  332 RSQKLDALEKEFIKEEdlaSKYDQLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIRELSEKNIHLQSSRDQALSELRE 411
Cdd:TIGR04523 466 LETQLKVLSRSINKIK---QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD 542

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  412 CELLLstSKAEAGVAIKKLKEEILSLEERIEVLRVANEN--SKQFEKSDNLENYEQLQQE 469
Cdd:TIGR04523 543 LEDEL--NKDDFELKKENLEKEIDEKNKEIEELKQTQKSlkKKQEEKQELIDQKEKEKKD 600
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
327-481 4.17e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 4.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 327 RKLESRSQKLDALEKEFIKEEDLASKYDQLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIR--ELSEKNIHLQSSRDQ 404
Cdd:COG4717   64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAE 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254568998 405 ALSELRECELLLSTSKaEAGVAIKKLKEEILSLEERIEVLRVANENSKQFEKSDNLENYEQLQQEFSHSQENWKLIE 481
Cdd:COG4717  144 LPERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 265-560 6.06e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 6.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   265 NRDSVINNLQKKLEAKELQVKELLEEgmkLSSNEVSLLQT-VKRLKQENNSLANELNN----ASEINRKLESRSQKLDAL 339
Cdd:TIGR02169  755 NVKSELKELEARIEELEEDLHKLEEA---LNDLEARLSHSrIPEIQAELSKLEEEVSRiearLREIEQKLNRLTLEKEYL 831

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   340 EKEFIKEEDLASKYDQLKNEFQQKEKELKKvQVREtnLDNKLHNANQEIRELSEKNIHLQSSRDQALSELRECElllsts 419
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIENLNG-KKEE--LEEELEELEAALRDLESRLGDLKKERDELEAQLRELE------ 902

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   420 kaeagVAIKKLKEEILSLEERIEVLRVANENskqfeKSDNLENYEQLQQEFSHSQENWKLIEDGYirkisslesdisssk 499
Cdd:TIGR02169  903 -----RKIEELEAQIEKKRKRLSELKAKLEA-----LEEELSEIEDPKGEDEEIPEEELSLEDVQ--------------- 957

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254568998   500 tkeqqsgKQVKALTSEIKELSRDNTRLINDVQVLSKDISVLKKELNLKNAEIKALNETLEN 560
Cdd:TIGR02169  958 -------AELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 350-577 6.78e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 6.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 350 ASKYDQLKNEFQQKEKEL-----KKVQVRETNLDNKLHNANQEIRELSEKNIHLQSSRDQA----------LSELRECEL 414
Cdd:COG1196  212 AERYRELKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELrleleeleleLEEAQAEEY 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 415 LLSTSKAEAGVAIKKLKEEILSLEERIEVLRvANENSKQFEKSDNLENYEQLQQEFSHSQENWKLIEDgyirKISSLESD 494
Cdd:COG1196  292 ELLAELARLEQDIARLEERRRELEERLEELE-EELAELEEELEELEEELEELEEELEEAEEELEEAEA----ELAEAEEA 366

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 495 ISSSKTKEQQSGKQVKALTSEIKELSRDNTRLINDVQVLSKDISVLKKELNLKNAEIKALNETLENKVNTFDLEKKRLIR 574
Cdd:COG1196  367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446


                 ...
gi 254568998 575 KLE 577
Cdd:COG1196  447 AAE 449
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 347-589 1.16e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 347 EDLASKYDQLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIRELSEKNIHLQSSRDQALSELREcellLSTSKAEAGVA 426
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE----LEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 427 IKKLKEEIlsleerIEVLRVANENSKQfEKSDNLENYEQLQQeFSHSQENWKLIEDGYIRKISSLESDISSSKTKEQQSG 506
Cdd:COG4942   99 LEAQKEEL------AELLRALYRLGRQ-PPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 507 KQVKALTSEIKELSRDNTRLINDVQVLSKDISVLKKELNLKNAEIKALN---ETLENKVNTFDLEKKRLIRKLEVKNFPS 583
Cdd:COG4942  171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQqeaEELEALIARLEAEAAAAAERTPAAGFAA 250


                 ....*.
gi 254568998 584 SDPGIP 589
Cdd:COG4942  251 LKGKLP 256
PLN02939 PLN02939
transferase, transferring glycosyl groups
 178-595 1.75e-05

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 48.36  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 178 ATTSKPKRLTLQERLKLAAQTKAKKKREqketlgSALGASFHGAESPSSDLTDSEALKINAPVPSRTPISTPVTGATPSS 257
Cdd:PLN02939  15 GPIRSRAPFYLPSRRRLAVSCRARRRGF------SSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 258 TPLSFVNNRDSVINNLQKKLEAKELQVKELLEEGMKLSSNEVSLLQTVKRLKQENNSLANElnnaseinrkleSRSQKLD 337
Cdd:PLN02939  89 KSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQ------------ARLQALE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 338 ALEKEFIKEEDLASKYDQLKNEFQQKEKELK---KVQVRETNLDNKLHNANQEIRELSEKNIHLQSSRDQALSELRECEL 414
Cdd:PLN02939 157 DLEKILTEKEALQGKINILEMRLSETDARIKlaaQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENM 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 415 LLSTSkaeagvaIKKLKEEILSL---EERIEVLrvanENSKQFEKSdnleNYEQLQQEFSHSQEN-WKLIE---DGYIRK 487
Cdd:PLN02939 237 LLKDD-------IQFLKAELIEVaetEERVFKL----EKERSLLDA----SLRELESKFIVAQEDvSKLSPlqyDCWWEK 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 488 ISSLESDISSSKTKEQQSG----------KQVKALTSEIKE--LSRDNTRLindVQVLSKDISVLKKELNLKNAEIKALN 555
Cdd:PLN02939 302 VENLQDLLDRATNQVEKAAlvldqnqdlrDKVDKLEASLKEanVSKFSSYK---VELLQQKLKLLEERLQASDHEIHSYI 378

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 254568998 556 ETLENKVNTFDLEKKRLIRKLEVKNFPSSDPGIPSDSLSR 595
Cdd:PLN02939 379 QLYQESIKEFQDTLSKLKEESKKRSLEHPADDMPSEFWSR 418
Macoilin pfam09726
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ...
 275-457 2.70e-05

Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.


Pssm-ID: 462859 [Multi-domain]  Cd Length: 670  Bit Score: 47.54  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  275 KKLEAkELQVKELLEEGMK-----LSSNEVSLLQTVKRLKQENNSLANELNNASeinrklesrSQKldalekefikeedl 349
Cdd:pfam09726 405 KKLKA-ELQASRQTEQELRsqissLTSLERSLKSELGQLRQENDLLQTKLHNAV---------SAK-------------- 460

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  350 askyDQLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIRELSEKNIHlqsSRDQALSELRECELLLSTSKAEAGVAIKK 429
Cdd:pfam09726 461 ----QKDKQTVQQLEKRLKAEQEARASAEKQLAEEKKRKKEEEATAAR---AVALAAASRGECTESLKQRKRELESEIKK 533

                         170       180
                  ....*....|....*....|....*...
gi 254568998  430 LKEEILSLEERIEVLRVANENSKQFEKS 457
Cdd:pfam09726 534 LTHDIKLKEEQIRELEIKVQELRKYKES 561
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
274-442 3.15e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  274 QKKLEAKELQVKEL------LEEGMKLSSNEVSLLQTVKRLKQENNSLANELNNASEINRKLESRSQKLDALEKEFIKEE 347
Cdd:COG4913   609 RAKLAALEAELAELeeelaeAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLA 688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  348 DLASKYDQLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIRELSEKNIHLQSSRDQALSELRE-------CELLLSTSK 420
Cdd:COG4913   689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaaalGDAVERELR 768

                         170       180
                  ....*....|....*....|..
gi 254568998  421 AEAGVAIKKLKEEILSLEERIE 442
Cdd:COG4913   769 ENLEERIDALRARLNRAEEELE 790
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 392-754 4.96e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 4.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   392 SEKNIHLQSSRDQALSELRECELLLSTSKAEAGVAIKKLKEEILSLEERIEVLRVAnENSKQFEKSDNLENYEQLQQEFS 471
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE-LEELSRQISALRKDLARLEAEVE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   472 HSQENWKLIEdgyiRKISSLESDISSSKTKEQQSGKQVKALTSEIKELSRDNTRLINDVQVLSKDISVLKKELNLKNAEI 551
Cdd:TIGR02168  744 QLEERIAQLS----KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   552 KALNETLENKVNTFDLEKKRLIRKLEVKNFPSSDPGIPSDSLSRERSLGDISSTSITSSLNptnnsshnsfqlgESSSRR 631
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN-------------ERASLE 886

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   632 ISTASILDNSFTNDSDVRTIDDSGHPTNHAMDMLTSQLRSLELQVSKLKTE----NKYLAEEKKGLTQEIVKLMKLNENS 707
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRidnlQERLSEEYSLTLEEAEALENKIEDD 966

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 254568998   708 KAY-HHEIETLNQQLQ-------DSKTEYEnalillgEKSELVEELRADVEDLKD 754
Cdd:TIGR02168  967 EEEaRRRLKRLENKIKelgpvnlAAIEEYE-------ELKERYDFLTAQKEDLTE 1014
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
265-585 1.18e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 265 NRDSVINNLQKKLEAKELQVKEL------LEEGMKLSSNEVSLLQTVKRLKQENNSLANELNNASEINRKLESRSQKLDA 338
Cdd:PRK03918 263 ELEERIEELKKEIEELEEKVKELkelkekAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 339 LEKefiKEEDLASKYDQLK------NEFQQKEKELKKVQVRETNLDnkLHNANQEIRELSEKNIHLQSSRDQALSELREc 412
Cdd:PRK03918 343 LKK---KLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGE- 416

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 413 ellLSTSKAEAGVAIKKLKE---------EILSLEERIEVLRVANENSKQFEKSdnLENYEQLQQEFSHSQENWKLIEDG 483
Cdd:PRK03918 417 ---LKKEIKELKKAIEELKKakgkcpvcgRELTEEHRKELLEEYTAELKRIEKE--LKEIEEKERKLRKELRELEKVLKK 491

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 484 YIRKISSLESDISSSKTKEQQSGKQVKALTSEIKELSRDNTRLINdvqvLSKDISVLKKELNLKNAEIKALnETLENKVN 563
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK----LKGEIKSLKKELEKLEELKKKL-AELEKKLD 566

                        330       340
                 ....*....|....*....|..
gi 254568998 564 TFDLEKKRLIRKLEVKNFPSSD 585
Cdd:PRK03918 567 ELEEELAELLKELEELGFESVE 588
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 264-580 1.56e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.40  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  264 NNRDSVINNLQKKLEAKELQVKELLEEGMKLSSNEVSLLQTVKRLKQENNSLANELN-----------NASEINRKLESR 332
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNllekeklniqkNIDKIKNKLLKL 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  333 SQKLDALEKEFIKEEDLASKYDQLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIRELSEKNIHL-------QSSRDQA 405
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIkkqlsekQKELEQN 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  406 LSELRECELLLSTSKAE--------AGVAIKKLKEEILSLEERIEVLRVANENSKQFEKSDNlENYEQLQQEFSHSQENW 477
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEisdlnnqkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLN-EQISQLKKELTNSESEN 358

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  478 KLIEdgyiRKISSLESDISSSKTKEQQSGKQVKALTSEIKELSRDNTRLINDVQVLSKDISVLKKELNLKNAEIKALNET 557
Cdd:TIGR04523 359 SEKQ----RELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434

                         330       340
                  ....*....|....*....|....
gi 254568998  558 LENKVNTF-DLEKKRLIRKLEVKN 580
Cdd:TIGR04523 435 IIKNNSEIkDLTNQDSVKELIIKN 458
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
260-481 5.62e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 5.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 260 LSFVNNRdsvINNLQKKLEAKELQVKELLEEgMKLSSNEVSLLQTVKRLKQENNSLANELNNASEINRKLESRSQKLdAL 339
Cdd:COG3206  177 LEFLEEQ---LPELRKELEEAEAALEEFRQK-NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL-GS 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 340 EKEFIKEEDLASKYDQLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIRELSEKnihLQSSRDQALSELRECELLLSTS 419
Cdd:COG3206  252 GPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ---LQQEAQRILASLEAELEALQAR 328

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254568998 420 KAEAGVAIKKLKEEILSL---EERIEVL-RVANENSKQFEksDNLENYEQLQQEFSHSQENWKLIE 481
Cdd:COG3206  329 EASLQAQLAQLEARLAELpelEAELRRLeREVEVARELYE--SLLQRLEEARLAEALTVGNVRVID 392
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 270-445 7.42e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 7.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 270 INNLQKKLEAKELQVKELLEEGMKLSSNEVSLLQTVKRLKQENNSLANELNNA----SEINRKLESRSQKLDALEKEFIK 345
Cdd:COG4942   22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALeqelAALEAELAELEKEIAELRAELEA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 346 EEDL----------ASKYDQLK-----NEFQQKEKELKKVQVRETNLDNKLHNANQEIRELSEKNIHLQSSRDQ---ALS 407
Cdd:COG4942  102 QKEElaellralyrLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEleaLLA 181

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 254568998 408 ELRECELLLSTSKAEAGVAIKKLKEEILSLEERIEVLR 445
Cdd:COG4942  182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
46 PHA02562
endonuclease subunit; Provisional
 367-574 8.72e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.69  E-value: 8.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 367 LKKVQVRETN-----LDNKLHNANQEIrELSEKNI-HLQSSRDQALSELREcelLLSTSKAEAgvaiKKLKEEILSLEER 440
Cdd:PHA02562 171 LNKDKIRELNqqiqtLDMKIDHIQQQI-KTYNKNIeEQRKKNGENIARKQN---KYDELVEEA----KTIKAEIEELTDE 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 441 IEVLRVANE---------NSKQFEKSDNLENYEQLQ-------------QEFSHSQENWKLIED------GYIRKISSLE 492
Cdd:PHA02562 243 LLNLVMDIEdpsaalnklNTAAAKIKSKIEQFQKVIkmyekggvcptctQQISEGPDRITKIKDklkelqHSLEKLDTAI 322

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 493 SDISSSKTKEQQSGKQVKALTSEIKELSRDNTRLINDVQVLSKDISVLKKELNLKNAEIKALNETLENKVNTF-DLEKKR 571
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKsELVKEK 402


                 ...
gi 254568998 572 LIR 574
Cdd:PHA02562 403 YHR 405
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 263-560 1.89e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  263 VNNRDSVINNLQKKLEAKELQVKELLEEGMKLSSNEVSLLQTVKRLKQENNSLANELNNASEINRKLESRSQKLDaLEKE 342
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ-QEKE 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  343 FIKEE---------DLASKYDQLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIRELSEKNIHLQSSRDQALSELREce 413
Cdd:TIGR04523 423 LLEKEierlketiiKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK-- 500

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  414 llLSTSKAEAGVAIKKLKEEILSLEERIEVLRvaNENSKQFEKSDNLENyEQLQQEFSHSQENWKLIEDGYIRKISSLES 493
Cdd:TIGR04523 501 --LNEEKKELEEKVKDLTKKISSLKEKIEKLE--SEKKEKESKISDLED-ELNKDDFELKKENLEKEIDEKNKEIEELKQ 575

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254568998  494 DISSSKTKEQQSGKQVKALTSEIKELSRDNTRLINDVQVLSKDISVLKKELNLKNAEIKALNETLEN 560
Cdd:TIGR04523 576 TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNK 642
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
298-445 2.18e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  298 EVSLLQtvKRLKQENNSLANELNNASEINRKLESRSQKLDALEKEfIKEEDLASKyDQLKNEFQQKEKELKKVQVRETNL 377
Cdd:COG4913   289 RLELLE--AELEELRAELARLEAELERLEARLDALREELDELEAQ-IRGNGGDRL-EQLEREIERLERELEERERRRARL 364

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254568998  378 DNKLHN----ANQEIRELSEKNIHLQSSRDQALSELRECELLLstskAEAGVAIKKLKEEILSLEERIEVLR 445
Cdd:COG4913   365 EALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEAL----AEAEAALRDLRRELRELEAEIASLE 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 270-441 2.33e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   270 INNLQKKLEAKELQVKELLEEGMKLSSNEVSLLQTVKRLKQENNSLANELNNASEINRKLESrsqkldALEKEFIKEEDL 349
Cdd:TIGR02168  798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA------EIEELEELIEEL 871

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   350 ASKYDQLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIRELseknihlqssrDQALSELREcelllstSKAEAGVAIKK 429
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL-----------RRELEELRE-------KLAQLELRLEG 933

                          170
                   ....*....|..
gi 254568998   430 LKEEILSLEERI 441
Cdd:TIGR02168  934 LEVRIDNLQERL 945
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 267-460 2.67e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.07  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 267 DSVINNLQKKLEAKELQVKELLEEGMKLSSNEVSLLQTVKRLKQENN---SLANELNN------ASEINRKLESRSQKLD 337
Cdd:PRK05771  85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNfdlDLSLLLGFkyvsvfVGTVPEDKLEELKLES 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 338 ALEKEFIKEEDLASKY---DQLKNEFQQKEKELKKVQVRETNLDNKLHnANQEIRELSEKNIHLQSSRDQALSELREcel 414
Cdd:PRK05771 165 DVENVEYISTDKGYVYvvvVVLKELSDEVEEELKKLGFERLELEEEGT-PSELIREIKEELEEIEKERESLLEELKE--- 240

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 254568998 415 llstskaeagvAIKKLKEEILSLEERIEVLRVANENSKQFEKSDNL 460
Cdd:PRK05771 241 -----------LAKKYLEELLALYEYLEIELERAEALSKFLKTDKT 275
COG5022 COG5022
Myosin heavy chain [General function prediction only];
262-599 2.71e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.22  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  262 FVNNRDSVINNLQKKLEaKELQVKELLEEGMKLSS---------------------NEVSLLQTVKRLKQENNSL----- 315
Cdd:COG5022   811 EYRSYLACIIKLQKTIK-REKKLRETEEVEFSLKAevliqkfgrslkakkrfsllkKETIYLQSAQRVELAERQLqelki 889

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  316 -ANELNNASEINRKLES------RSQKLDALEKEFIKEEDLAsKYDQLKNEFQQKEKELKKVQvrETNLDNKLHNANQEI 388
Cdd:COG5022   890 dVKSISSLKLVNLELESeiielkKSLSSDLIENLEFKTELIA-RLKKLLNNIDLEEGPSIEYV--KLPELNKLHEVESKL 966

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  389 RELSEKNIHLQSSRDQALSELR-ECELLLSTSKAEAGVAIKK--LKEEILSLEER-IEVLRVANENSKQFEKSDNLENYE 464
Cdd:COG5022   967 KETSEEYEDLLKKSTILVREGNkANSELKNFKKELAELSKQYgaLQESTKQLKELpVEVAELQSASKIISSESTELSILK 1046

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  465 QLQQEFSHSQENWKLIEDGYIRKISSLESDISSSKTKEQQSGKQVKALTSEIKELSRDNTRLINDVQVLSKDISVLKKEL 544
Cdd:COG5022  1047 PLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLN 1126

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 254568998  545 NLKNAE--IKALNETLENKVNTFDLEKKRLIRKLEVKNFPSSDPGIPSDSLSRERSL 599
Cdd:COG5022  1127 LLQEISkfLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLY 1183
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 266-475 2.83e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   266 RDSVINNLQKKLEAKELQVKELLEEGMKLSSNEVSLLQT---------------VKRLKQENNSLANELNNASEINRKLE 330
Cdd:TIGR02169  256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkigeleaeiaslersIAEKERELEDAEERLAKLEAEIDKLL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   331 SRSQKLD------ALEKEFIKEE--DLASKYDQLKNEFQQKEK-------ELKKVQVRETNLDNKLHNANQEIRELSEKN 395
Cdd:TIGR02169  336 AEIEELEreieeeRKRRDKLTEEyaELKEELEDLRAELEEVDKefaetrdELKDYREKLEKLKREINELKRELDRLQEEL 415

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   396 IHLQSSRDQALSELRECELLLSTSKAEAGVAIKKLKEEILSLEERIEVLRVANEnskqfEKSDNLENYEQLQQEFSHSQE 475
Cdd:TIGR02169  416 QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ-----ELYDLKEEYDRVEKELSKLQR 490
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 271-578 2.84e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  271 NNLQKKLEAKELQvkelLEEGMKLSSNEVSLLQTVK-RLKQENNSLANELNNasEINRKLESRSQKLDALEKEFIKEEdl 349
Cdd:TIGR04523 263 NKIKKQLSEKQKE----LEQNNKKIKELEKQLNQLKsEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQNQISQNN-- 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  350 aSKYDQLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIRELSEKNIHLQSSRDQALSELRECELLLSTSKAEAG---VA 426
Cdd:TIGR04523 335 -KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQqkdEQ 413

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  427 IKKLKEEILSLEERIEVLRvaNENSKQFEKSDNLENYEQlqqEFSHSQENWKLIEDGYIRKISSLESDISSSKTKEQQSG 506
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLK--ETIIKNNSEIKDLTNQDS---VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ 488

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254568998  507 KQVKALTSEIKELSRDNTRLINDVQVLSKDISVLKKELNLKNAEIKALNE---TLENKVNTFDLEKKRLIRKLEV 578
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESkisDLEDELNKDDFELKKENLEKEI 563
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 266-448 3.16e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.39  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   266 RDSVINNLQKKLEakelQVKELLEEGMKLSSNEVSLLQTVK-RLKQENNSLANELNNASEINRKLESRSQKLDALEKEFI 344
Cdd:smart00787 138 RMKLLEGLKEGLD----ENLEGLKEDYKLLMKELELLNSIKpKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKL 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   345 KEEDLASKYdqLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIRELSEKnihLQSSRDQALSELRECELLLSTSKAEAG 424
Cdd:smart00787 214 KKLLQEIMI--KVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKK---LEQCRGFTFKEIEKLKEQLKLLQSLTG 288

                          170       180
                   ....*....|....*....|....
gi 254568998   425 VAIKKLKEEILSLEERIEVLRVAN 448
Cdd:smart00787 289 WKITKLSGNTLSMTYDREINLVFD 312
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 271-579 3.81e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.86  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  271 NNLQKKLEAKELQVKEL-LEEGMKLSSNEVSLLQTVKRLKQENNSLANELNNASEINRKLESRSQKLDALEKEFIKE-ED 348
Cdd:pfam05483 375 NEDQLKIITMELQKKSSeLEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEiHD 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  349 LASKYDQLKNEFQQKEKELK--KVQVRETNLDNKLHNANQEIRELSEKNIhLQSSRDQALSELRECELLLSTSKAEagva 426
Cdd:pfam05483 455 LEIQLTAIKTSEEHYLKEVEdlKTELEKEKLKNIELTAHCDKLLLENKEL-TQEASDMTLELKKHQEDIINCKKQE---- 529

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  427 iKKLKEEILSLEERIEVLRvaneNSKQFEKSDNLENYEQLQQEFSHSQENWKLIEDGYIRKisslESDISSSKTKEQQSG 506
Cdd:pfam05483 530 -ERMLKQIENLEEKEMNLR----DELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKK----EKQMKILENKCNNLK 600

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254568998  507 KQVKALTSEIKELSRDNtrlindvQVLSKDISVLKKELNLKNAEIKALNETLENKVNTFDLEKKRLIRKLEVK 579
Cdd:pfam05483 601 KQIENKNKNIEELHQEN-------KALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 270-563 4.21e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  270 INNLQKKLEAKELQVKELLEEGMKLSSNEVSLLQTVKRLKQENNSLANELNNASEINRKLESRSQKLDALEKEFIKEED- 348
Cdd:TIGR04523  42 LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNk 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  349 LASKYDQLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIRELSEKnihlqssrdqaLSELRECELLLSTSKAEAGVAIK 428
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQ-----------KEELENELNLLEKEKLNIQKNID 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998  429 KLKEEILSLEERIEVLRVANENSKQFEKSDNLENYEQLQQEFSHSQENWKLIEdgYIRKISSLESDISSSKTKEQQSGKQ 508
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE--KTTEISNTQTQLNQLKDEQNKIKKQ 268

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 254568998  509 VKALTSEIKELSRDNTRLINDVQVLSKDISVLKKElnlKNAEI-KALNETLENKVN 563
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ---KEQDWnKELKSELKNQEK 321
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
275-456 4.37e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 4.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 275 KKLEAKELQVKELLEEGMKLSSNEVSLLQTVKRLKQENNSLANELNNA------SEINRKLESRSQKLDALEKEFIKEED 348
Cdd:COG4717   81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyqelEALEAELAELPERLEELEERLEELRE 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 349 LASKYDQLKNEFQQKEKELKKVQVRETNldnklhNANQEIRELSEKNIHLQSSRDQALSELrecelllstskaeagvaiK 428
Cdd:COG4717  161 LEEELEELEAELAELQEELEELLEQLSL------ATEEELQDLAEELEELQQRLAELEEEL------------------E 216

                        170       180
                 ....*....|....*....|....*...
gi 254568998 429 KLKEEILSLEERIEVLRVANENSKQFEK 456
Cdd:COG4717  217 EAQEELEELEEELEQLENELEAAALEER 244
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 270-580 4.68e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.42  E-value: 4.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   270 INNLQKKLEAKELQVKELLEEGMKLSSNEVSLLQTVKRLKQENNSLA-------------NELNNASEINRKLESRSQKL 336
Cdd:TIGR00606  610 INNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAmlagatavysqfiTQLTDENQSCCPVCQRVFQT 689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   337 DALEKEFIKeeDLASKYDQLKNEFQQKEKELKKVQVRETNL-------DNKLHNANQEIRELSEKNIHLQSSRDQALSEL 409
Cdd:TIGR00606  690 EAELQEFIS--DLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   410 RECELLLSTSKAEAGVA---------IKKLKEEILSLEERIEvlrvanENSKQFEKSDNLENYEQLQQEFSHSQENWkli 480
Cdd:TIGR00606  768 EEQETLLGTIMPEEESAkvcltdvtiMERFQMELKDVERKIA------QQAAKLQGSDLDRTVQQVNQEKQEKQHEL--- 838

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   481 edgyiRKISSLESDISSSKTKEQQSGKQVKALTSEIKELSRDNTRLINDVQVLSKDISVLKKELNLKNAEIKALNET--- 557
Cdd:TIGR00606  839 -----DTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdsp 913

                          330       340
                   ....*....|....*....|...
gi 254568998   558 LENKVNTFDLEKKRLIRKLEVKN 580
Cdd:TIGR00606  914 LETFLEKDQQEKEELISSKETSN 936
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 277-560 4.84e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 4.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   277 LEAKELQVKELLEEGMKLSSNEVSLLQTVKRLKQENNSLANELNNASEINRKLESrsqkldaLEKEfikeEDLASKYDQL 356
Cdd:TIGR02168  150 IEAKPEERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKS-------LERQ----AEKAERYKEL 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   357 KNEFQQKEKELKKVQVREtnLDNKLHNANQEIRELseknihlQSSRDQALSELRECELLLSTskaeagvaikkLKEEILS 436
Cdd:TIGR02168  219 KAELRELELALLVLRLEE--LREELEELQEELKEA-------EEELEELTAELQELEEKLEE-----------LRLEVSE 278

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   437 LEERIEVLRVANENSKQfEKSDnLENYEQLQQEfshsqenwkliedgyirkisslesdisssktKEQQSGKQVKALTSEI 516
Cdd:TIGR02168  279 LEEEIEELQKELYALAN-EISR-LEQQKQILRE-------------------------------RLANLERQLEELEAQL 325

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 254568998   517 KELSRDNTRLINDVQVLSKDISVLKKELNLKNAEIKALNETLEN 560
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 260-469 5.21e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 40.30  E-value: 5.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 260 LSFVNNRDSVINNLQK--KLEAKELQVKELLEEGMKLSSN--EVS-LLQTVKRLKQENNSLANELNNAS--EINRKLESR 332
Cdd:PRK05771  12 VTLKSYKDEVLEALHElgVVHIEDLKEELSNERLRKLRSLltKLSeALDKLRSYLPKLNPLREEKKKVSvkSLEELIKDV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 333 SQKLDALEKEFikeEDLASKYDQLKNEFQQKEKELKKVQ------------------------VRETNLDNKLHNANQ-- 386
Cdd:PRK05771  92 EEELEKIEKEI---KELEEEISELENEIKELEQEIERLEpwgnfdldlslllgfkyvsvfvgtVPEDKLEELKLESDVen 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 387 --EIRELSEKN----IHLQSSRDQALSELRECELL-LSTS-KAEAGVAIKKLKEEILSLEERIEVLRVANENSKQFEKSD 458
Cdd:PRK05771 169 veYISTDKGYVyvvvVVLKELSDEVEEELKKLGFErLELEeEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEE 248

                        250
                 ....*....|.
gi 254568998 459 NLENYEQLQQE 469
Cdd:PRK05771 249 LLALYEYLEIE 259
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
275-456 8.45e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 8.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 275 KKLEAKELQVKELLEEGMKLSSNEVSLLQTVKRLKQENNSLA---NELNNA----SEINRKLESRSQK-LDALEKEFIKE 346
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAeleKKLDELeeelAELLKELEELGFEsVEELEERLKEL 597

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998 347 EDLASKYDQLKNEFQQKEKELKKVQVRETNLD---NKLHNANQEIRELSEKNIHLQSSRDQALSElRECELLLSTSKAEA 423
Cdd:PRK03918 598 EPFYNEYLELKDAEKELEREEKELKKLEEELDkafEELAETEKRLEELRKELEELEKKYSEEEYE-ELREEYLELSRELA 676

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 254568998 424 GV-----AIKKLKEEILS----LEERIEVLRVANENSKQFEK 456
Cdd:PRK03918 677 GLraeleELEKRREEIKKtlekLKEELEEREKAKKELEKLEK 718
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 270-577 9.76e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 39.33  E-value: 9.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   270 INNLQKKLEAKELQVKEL--LEEGMKlSSNEVSLLQTVKRLKQENNSLanelNNASEINRKLESRSQKLDALEKEFIKE- 346
Cdd:pfam15921  414 IDHLRRELDDRNMEVQRLeaLLKAMK-SECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKk 488

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   347 ---EDLASKYDQLKNEFQQKEKELKKVQVRETNLDNKLHNANQEIRELSEKNIHLQSSRdqalselRECElLLSTSKAEA 423
Cdd:pfam15921  489 mtlESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQ-------TECE-ALKLQMAEK 560

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568998   424 GVAIKKLKEEILSLEERI-EVLRVANE---NSKQFEKSDNLENYEqlQQEFSHSQENwkliEDGYIRKISSLESDISSSK 499
Cdd:pfam15921  561 DKVIEILRQQIENMTQLVgQHGRTAGAmqvEKAQLEKEINDRRLE--LQEFKILKDK----KDAKIRELEARVSDLELEK 634

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254568998   500 TKEQQSGKQvkaLTSEIKELSRDNTRLINDVQVLSKDISVLKKELNLKNAEIKALNETLENKVNTFDLEKKRLIRKLE 577
Cdd:pfam15921  635 VKLVNAGSE---RLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELE 709
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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